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Details on Person UniProt:Q92878 RAD50

Class:Id	ReferenceGeneProduct:75159
_chainChangeLog	chain:1-1312 added on Sat February 7 2015
_displayName	UniProt:Q92878 RAD50
_timestamp	2025-02-21 19:00:52
chain	chain:1-1312
checksum	1F208C3817FC41FC
comment	FUNCTION Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28134932, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:15064416, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:11741547, PubMed:9590181, PubMed:9651580, PubMed:9705271). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (PubMed:11741547, PubMed:12805565, PubMed:28134932). RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888).CATALYTIC ACTIVITY ATP + H2O = ADP + phosphate + H(+)COFACTOR Binds 1 zinc ion per homodimer.SUBUNIT Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single NBN (PubMed:10839544, PubMed:26215093, PubMed:28867292, PubMed:36577401, PubMed:8756642, PubMed:9590181, PubMed:9705271). The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:36577401). As part of the MRN complex, interacts with MCM8 and MCM9; the interaction recruits the complex to DNA repair sites (PubMed:26215093). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (PubMed:10783165). Found in a complex with TERF2 (PubMed:10888888). Interacts with RINT1 (PubMed:11096100). Interacts with BRCA1 via its N-terminal domain (PubMed:10426999). Interacts with DCLRE1C/Artemis (PubMed:15456891, PubMed:15723659). Interacts with MRNIP (PubMed:27568553). Interacts with CYREN (via XLF motif) (By similarity). Interacts with C1QBP and MRE11; interaction takes place in absence of DNA damage to form the MRC (MRE11-RAD50-C1QBP) complex that inhibits the activity of MRE11 (PubMed:31353207).SUBUNIT (Microbial infection) Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970).INTERACTION Localizes to discrete nuclear foci after treatment with genotoxic agents (PubMed:10783165, PubMed:26215093). Localizes to DNA double-strand breaks (DSBs) (PubMed:15916964, PubMed:21757780).ALTERNATIVE PRODUCTS Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts.DOMAIN The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer.PTM Phosphorylation at Ser-635 by ATM in response to DNA damage is required for double-strand break (DSB) repair.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the SMC family. RAD50 subfamily.SEQUENCE CAUTION Contaminating sequence. Potential poly-A sequence.
created	[InstanceEdit:75141] Matthews, L, 2003-08-11 05:43:00
description	recommendedName: DNA repair protein RAD50 shortName evidence="40"hRAD50 ecNumber evidence="26 35 43"3.6.-.-
geneName	RAD50
identifier	Q92878
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Alternative splicing ATP-binding Cell cycle Chromosome Coiled coil DNA damage DNA repair Host-virus interaction Hydrolase Magnesium Meiosis Metal-binding Nucleotide-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Telomere Zinc
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
name	RAD50
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8998546] ENSEMBL:ENSG00000113522 RAD50 [Homo sapiens]
secondaryIdentifier	RAD50_HUMAN B9EGF5 O43254 Q6GMT7 Q6P5X3 Q9UP86
sequenceLength	1312
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:244695] UniProt:Q92878-2 RAD50 [Homo sapiens] [ReferenceIsoform:244696] UniProt:Q92878-3 RAD50 [Homo sapiens] [ReferenceIsoform:412509] UniProt:Q92878-1 RAD50 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:75160] RAD50 [nucleoplasm] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:Q92878 RAD50 (75159)